Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme

2016 ◽  
Vol 9 (2) ◽  
pp. 581-594 ◽  
Author(s):  
Patrícia Raleiras ◽  
Namita Khanna ◽  
Hélder Miranda ◽  
Lívia S. Mészáros ◽  
Henning Krassen ◽  
...  
Keyword(s):  
Point Mutation ◽  
Epr Spectroscopy ◽  
Electron Flow ◽  
Single Point ◽  
Single Point Mutation ◽  
Uptake Hydrogenase ◽  
Nostoc Punctiforme

The uptake hydrogenase HupSL became a H2 producer in N. punctiforme after modifying the proximal FeS cluster with the single point mutation C12P.

scholarly journals Structural basis for a complex I mutation that blocks pathological ROS production

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Zhan Yin ◽  
Nils Burger ◽  
Duvaraka Kula-Alwar ◽  
Dunja Aksentijević ◽  
Hannah R. Bridges ◽  
...  
Keyword(s):  
Point Mutation ◽  
Complex I ◽  
Structural Changes ◽  
Ischemia Reperfusion ◽  
Single Point ◽  
Structural Basis ◽  
Single Point Mutation ◽  
Ros Production

AbstractMitochondrial complex I is central to the pathological reactive oxygen species (ROS) production that underlies cardiac ischemia–reperfusion (IR) injury. ND6-P25L mice are homoplasmic for a disease-causing mtDNA point mutation encoding the P25L substitution in the ND6 subunit of complex I. The cryo-EM structure of ND6-P25L complex I revealed subtle structural changes that facilitate rapid conversion to the “deactive” state, usually formed only after prolonged inactivity. Despite its tendency to adopt the “deactive” state, the mutant complex is fully active for NADH oxidation, but cannot generate ROS by reverse electron transfer (RET). ND6-P25L mitochondria function normally, except for their lack of RET ROS production, and ND6-P25L mice are protected against cardiac IR injury in vivo. Thus, this single point mutation in complex I, which does not affect oxidative phosphorylation but renders the complex unable to catalyse RET, demonstrates the pathological role of ROS production by RET during IR injury.

scholarly journals Single point mutation in adeno-associated viral vectors -DJ capsid leads to improvement for gene delivery in vivo

2016 ◽  
Vol 16 (1) ◽  
Author(s):  
Yingying Mao ◽  
Xuejun Wang ◽  
Renhe Yan ◽  
Wei Hu ◽  
Andrew Li ◽  
...  
Keyword(s):  
Gene Delivery ◽  
Point Mutation ◽  
Viral Vectors ◽  
Single Point ◽  
Single Point Mutation

scholarly journals A single point mutation in TFIIA suppresses NC2 requirement in vivo

2000 ◽  
Vol 19 (4) ◽  
pp. 672-682 ◽  
Author(s):  
Jun Xie ◽  
Martine Collart ◽  
Marc Lemaire ◽  
Gertraud Stelzer ◽  
Michael Meisterernst
Keyword(s):  
Point Mutation ◽  
Single Point ◽  
Single Point Mutation

Point mutation in acetolactate synthase confers sulfonylurea and imidazolinone herbicide resistance in spiny annual sow-thistle [Sonchus asper (L.) Hill]

2012 ◽  
Vol 92 (2) ◽  
pp. 303-309 ◽  
Author(s):  
Kee Woong Park ◽  
Judith M. Kolkman ◽  
Carol A. Mallory-Smith
Keyword(s):  
Amino Acid ◽  
Point Mutation ◽  
Herbicide Resistance ◽  
Single Point ◽  
Acetolactate Synthase ◽  
Amino Acid Sequences ◽  
Cross Resistance ◽  
Single Point Mutation ◽  
Sonchus Asper

Park, K. W., Kolkman, J. M. and Mallory-Smith, C. A. 2012. Point mutation in acetolactate synthase confers sulfonylurea and imidazolinone herbicide resistance in spiny annual sow-thistle [Sonchus asper (L.) Hill]. Can. J. Plant Sci. 92: 303–309. Suspected thifensulfuron resistant spiny annual sow-thistle was identified near Colfax, Washington, in two fields with a winter wheat and lentil rotation. Therefore, studies were conducted to examine resistance of spiny annual sow-thistle to thifensulfuron and cross-resistance to other acetolactate synthase inhibitors and to determine the physiological and molecular basis for herbicide resistance. Whole-plant bioassay confirmed that the biotype was highly resistant to the sulfonylurea (SU) herbicides, thifensulfuron, metsulfuron, and prosulfuron. The resistant (R) biotype was also highly resistant to the imidazolinone (IMI) herbicides, imazamox and imazethapyr. An in vivo acetolactate synthase (ALS) assay indicated that the concentrations of SU and IMI herbicides required for 50% inhibition (I50) were more than 10 times greater for R biotype compared with susceptible (S) biotype. Analysis of the nucleotide and predicted amino acid sequences for ALS genes demonstrated a single-point mutation from C to T at the als1 gene, conferring the substitution of the amino acid leucine for proline in the R biotype at position197. The results of this research indicate that the resistance of spiny annual sow-thistle to SU and IMI herbicides is due to on altered target site and caused by a point mutation in the als1 gene.

scholarly journals Mutation in Irf8 Gene (Irf8R294C) Impairs Type I IFN-Mediated Antiviral Immune Response by Murine pDCs

2021 ◽  
Vol 12 ◽  
Author(s):  
Annesa Das ◽  
Kuldeep Singh Chauhan ◽  
Himanshu Kumar ◽  
Prafullakumar Tailor
Keyword(s):  
Immune Response ◽  
Point Mutation ◽  
Single Point ◽  
Costimulatory Molecules ◽  
Type I Interferons ◽  
Single Point Mutation ◽  
Type I ◽  
Type I Ifn ◽  
Antiviral Immune Response

Plasmacytoid dendritic cells (pDCs) are the key producers of type I interferons (IFNs), thus playing a central role in initiating antiviral immune response. Besides robust type I IFN production, pDCs also act as antigen presenting cells post immunogenic stimulation. Transcription factor Irf8 is indispensable for the development of both pDC and cDC1 subset. However, the mechanism underlying the differential regulation by IRF8 in cDC1- and pDC-specific genomic architecture of developmental pathways still remains to be fully elucidated. Previous studies indicated that the Irf8R294C mutation specifically abrogates development of cDC1 without affecting that of pDC. In the present study using RNA-seq based approach, we have found that though the point mutation Irf8R294C did not affect pDC development, it led to defective type I IFN production, thus resulting in inefficient antiviral response. This observation unraveled the distinctive roles of IRF8 in these two subpopulations—regulating the development of cDC1 whereas modulating the functionality of pDCs without affecting development. We have reported here that Irf8R294C mutation also caused defect in production of ISGs as well as defective upregulation of costimulatory molecules in pDCs in response to NDV infection (or CpG stimulation). Through in vivo studies, we demonstrated that abrogation of type I IFN production was concomitant with reduced upregulation of costimulatory molecules in pDCs and increased NDV burden in IRF8R294C mice in comparison with wild type, indicating inefficient viral clearance. Further, we have also shown that Irf8R294C mutation abolished the activation of type I IFN promoter by IRF8, justifying the low level of type I IFN production. Taken together, our study signifies that the single point mutation in Irf8, Irf8R294C severely compromised type I IFN-mediated immune response by murine pDCs, thereby causing impairment in antiviral immunity.

scholarly journals Dominant-negative inhibition of pheromone receptor signaling by a single point mutation in the G protein α subunit. Vol. 279 (2004) 35287-35297

2005 ◽  
Vol 280 (33) ◽  
pp. 29988
Author(s):  
Yuh-Lin Wu ◽  
Shelley B. Hooks ◽  
T. Kendall Harden ◽  
Henrik G. Dohlman
Keyword(s):  
G Protein ◽  
Point Mutation ◽  
Single Point ◽  
Dominant Negative ◽  
Single Point Mutation ◽  
Receptor Signaling ◽  
Α Subunit ◽  
Pheromone Receptor ◽  
G Protein Α Subunit

scholarly journals A single point mutation converts a proton-pumping rhodopsin into a red-shifted, turn-on fluorescent sensor for chloride

2021 ◽  
Author(s):  
Jasmine N. Tutol ◽  
Jessica Lee ◽  
Hsichuan Chi ◽  
Farah N. Faizuddin ◽  
Sameera S. Abeyrathna ◽  
...  
Keyword(s):  
Point Mutation ◽  
Fluorescent Sensor ◽  
Single Point ◽  
Proton Pumping ◽  
Single Point Mutation ◽  
Turn On ◽  
Gloeobacter Violaceus

By utilizing laboratory-guided evolution, we have converted the fluorescent proton-pumping rhodopsin GR from Gloeobacter violaceus into GR1, a red-shifted, turn-on fluorescent sensor for chloride.

Sign in / Sign up

Export Citation Format

Share Document